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Database: UniProt
Entry: A0A0R3MJ00_9BRAD
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ID   A0A0R3MJ00_9BRAD        Unreviewed;       718 AA.
AC   A0A0R3MJ00;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE            EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN   ORFNames=CQ14_31640 {ECO:0000313|EMBL:KRR17437.1};
OS   Bradyrhizobium lablabi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR17437.1, ECO:0000313|Proteomes:UP000051660};
RN   [1] {ECO:0000313|EMBL:KRR17437.1, ECO:0000313|Proteomes:UP000051660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR17437.1,
RC   ECO:0000313|Proteomes:UP000051660};
RA   Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT   "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT   Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT   Spain.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC         pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359; EC=4.1.3.27;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036934};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5. {ECO:0000256|PIRNR:PIRNR036934}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRR17437.1}.
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DR   EMBL; LLYB01000122; KRR17437.1; -; Genomic_DNA.
DR   RefSeq; WP_057862102.1; NZ_LLYB01000122.1.
DR   AlphaFoldDB; A0A0R3MJ00; -.
DR   STRING; 722472.SAMN05444321_4054; -.
DR   OrthoDB; 9803598at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000051660; Unassembled WGS sequence.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR010112; TrpE-G_bact.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR01815; TrpE-clade3; 1.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF9; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PIRSF; PIRSF036934; TrpE-G; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF56322; ADC synthase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036934};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036934};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Lyase {ECO:0000256|PIRNR:PIRNR036934, ECO:0000313|EMBL:KRR17437.1};
KW   Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT   DOMAIN          123..203
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          247..499
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   DOMAIN          530..703
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        604
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        693
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        695
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   718 AA;  78582 MW;  A9A9DFB200C9CBDA CRC64;
     MNRTAFSLPE HSEYRTSGGL AISRTVEQFT GNAKRLDDLI ELLDRRRGVV LSSGTTVPGR
     YESFDLGFAD PPLVLETVGA NFSLTALNAR GEVLIAFLGD VLREPCVVIS EKSPTRLAGH
     IIRGAAPVEE DQRTRRASVM SLVRDLVAAL AANDDPLLGL FGAFAYDLVF QIEDLVQKRA
     READQRDIVL YVPDRLLAYD RATGRGVVLS YDFSWKGKST QGLPRDTAKS VYAKTPRQGF
     ADHAPGEYQA TVEVARAAFA RGDLFEAVPG QLFAEPCERS PAEVFQRLCR INPSPYGALM
     NLGDGEFLVS ASPEMFVRSD GRRVETCPIS GTIARGVDAI GDAEQIRQLL NSEKDEFELN
     MCTDVDRNDK ARVCVPGTIK VLARRQIETY SKLFHTVDHV EGMLRPGFDA LDAFLTHAWA
     VTVTGAPKLW AMQFVEDNER SSRRWYAGAI GAVNFDGSIN TGLTIRTIRM KDGLAEVRVG
     ATCLFDSDPA AEDRECQVKA AALFQALRGD APKPLSTFAP DATGSGRKVL LIDHDDSFVH
     MLADYFRQVG ANVTVVRHVH AQEMLKKNWD LLVLSPGPGR PEDFGISKTI GTALDRKLPI
     FGVCLGVQAI GEYFGGQLGQ LTQPAHGRPS RVQVRGGRLM QNLPNEIVIG RYHSLYVERD
     SVPDVLEVTA TTEDGVAMAI EHKTLPVGGV QFHPESLMSL GGEVGLRIVE NAFRLNAN
//
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